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Adaptation of Dinoroseobacter shibae to oxidative stress and the specific role of RirA
Dinoroseobacter shibae living in the photic zone of marine ecosystems is frequently exposed to oxygen that forms highly reactive species. Here, we analysed the adaptation of D. shibae to different kinds of oxidative stress using a GeLC-MS/MS approach. D. shibae was grown in artificial seawater mediu...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8007024/ https://www.ncbi.nlm.nih.gov/pubmed/33780465 http://dx.doi.org/10.1371/journal.pone.0248865 |
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author | Beier, Nicole Kucklick, Martin Fuchs, Stephan Mustafayeva, Ayten Behringer, Maren Härtig, Elisabeth Jahn, Dieter Engelmann, Susanne |
author_facet | Beier, Nicole Kucklick, Martin Fuchs, Stephan Mustafayeva, Ayten Behringer, Maren Härtig, Elisabeth Jahn, Dieter Engelmann, Susanne |
author_sort | Beier, Nicole |
collection | PubMed |
description | Dinoroseobacter shibae living in the photic zone of marine ecosystems is frequently exposed to oxygen that forms highly reactive species. Here, we analysed the adaptation of D. shibae to different kinds of oxidative stress using a GeLC-MS/MS approach. D. shibae was grown in artificial seawater medium in the dark with succinate as sole carbon source and exposed to hydrogen peroxide, paraquat or diamide. We quantified 2580 D. shibae proteins. 75 proteins changed significantly in response to peroxide stress, while 220 and 207 proteins were differently regulated by superoxide stress and thiol stress. As expected, proteins like thioredoxin and peroxiredoxin were among these proteins. In addition, proteins involved in bacteriochlophyll biosynthesis were repressed under disulfide and superoxide stress but not under peroxide stress. In contrast, proteins associated with iron transport accumulated in response to peroxide and superoxide stress. Interestingly, the iron-responsive regulator RirA in D. shibae was downregulated by all stressors. A rirA deletion mutant showed an improved adaptation to peroxide stress suggesting that RirA dependent proteins are associated with oxidative stress resistance. Altogether, 139 proteins were upregulated in the mutant strain. Among them are proteins associated with protection and repair of DNA and proteins (e. g. ClpB, Hsp20, RecA, and a thioredoxin like protein). Strikingly, most of the proteins involved in iron metabolism such as iron binding proteins and transporters were not part of the upregulated proteins. In fact, rirA deficient cells were lacking a peroxide dependent induction of these proteins that may also contribute to a higher cell viability under these conditions. |
format | Online Article Text |
id | pubmed-8007024 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-80070242021-04-07 Adaptation of Dinoroseobacter shibae to oxidative stress and the specific role of RirA Beier, Nicole Kucklick, Martin Fuchs, Stephan Mustafayeva, Ayten Behringer, Maren Härtig, Elisabeth Jahn, Dieter Engelmann, Susanne PLoS One Research Article Dinoroseobacter shibae living in the photic zone of marine ecosystems is frequently exposed to oxygen that forms highly reactive species. Here, we analysed the adaptation of D. shibae to different kinds of oxidative stress using a GeLC-MS/MS approach. D. shibae was grown in artificial seawater medium in the dark with succinate as sole carbon source and exposed to hydrogen peroxide, paraquat or diamide. We quantified 2580 D. shibae proteins. 75 proteins changed significantly in response to peroxide stress, while 220 and 207 proteins were differently regulated by superoxide stress and thiol stress. As expected, proteins like thioredoxin and peroxiredoxin were among these proteins. In addition, proteins involved in bacteriochlophyll biosynthesis were repressed under disulfide and superoxide stress but not under peroxide stress. In contrast, proteins associated with iron transport accumulated in response to peroxide and superoxide stress. Interestingly, the iron-responsive regulator RirA in D. shibae was downregulated by all stressors. A rirA deletion mutant showed an improved adaptation to peroxide stress suggesting that RirA dependent proteins are associated with oxidative stress resistance. Altogether, 139 proteins were upregulated in the mutant strain. Among them are proteins associated with protection and repair of DNA and proteins (e. g. ClpB, Hsp20, RecA, and a thioredoxin like protein). Strikingly, most of the proteins involved in iron metabolism such as iron binding proteins and transporters were not part of the upregulated proteins. In fact, rirA deficient cells were lacking a peroxide dependent induction of these proteins that may also contribute to a higher cell viability under these conditions. Public Library of Science 2021-03-29 /pmc/articles/PMC8007024/ /pubmed/33780465 http://dx.doi.org/10.1371/journal.pone.0248865 Text en © 2021 Beier et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Beier, Nicole Kucklick, Martin Fuchs, Stephan Mustafayeva, Ayten Behringer, Maren Härtig, Elisabeth Jahn, Dieter Engelmann, Susanne Adaptation of Dinoroseobacter shibae to oxidative stress and the specific role of RirA |
title | Adaptation of Dinoroseobacter shibae to oxidative stress and the specific role of RirA |
title_full | Adaptation of Dinoroseobacter shibae to oxidative stress and the specific role of RirA |
title_fullStr | Adaptation of Dinoroseobacter shibae to oxidative stress and the specific role of RirA |
title_full_unstemmed | Adaptation of Dinoroseobacter shibae to oxidative stress and the specific role of RirA |
title_short | Adaptation of Dinoroseobacter shibae to oxidative stress and the specific role of RirA |
title_sort | adaptation of dinoroseobacter shibae to oxidative stress and the specific role of rira |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8007024/ https://www.ncbi.nlm.nih.gov/pubmed/33780465 http://dx.doi.org/10.1371/journal.pone.0248865 |
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